Linked Life Data

7545917

Source:http://linkedlifedata.com/resource/pubmed/id/7545917

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1994-5-5
pubmed:databankReference
pubmed:abstractText
Endothelial-monocyte-activating polypeptide II (EMAP II) is a novel mediator isolated from conditioned medium of methylcholanthrene A-induced tumor cells which modulates properties of endothelial cells, mononuclear phagocytes (MPs), and polymorphonuclear leukocytes (PMNs) in vitro and induces an acute inflammatory response in vivo. A synthetic peptide comprising 15 residues from the N-terminal region (residues 6-20) was shown to induce directional migration of MPs and PMNs, with half-maximal effect at approximately 200-250 pM, whereas a peptide from the C terminus of EMAP II, as well as other irrelevant peptides, were without effect. Modulation of cellular phenotype by EMAP II-derived peptide was suggested by peptide-induced elevation of cytosolic free calcium concentration in fura-2-loaded MPs and PMNs and by stimulation of peroxidase release in PMNs. Consistent with these in vitro data, EMAP II-derived N-terminal peptide-albumin conjugates injected into the mouse footpad elicited inflammatory cell tissue infiltration, whereas albumin alone or EMAP II-derived C-terminal peptide conjugated to albumin incited little response. Binding of 125I-labeled EMAP II-derived peptide (residues 12-20) to MPs was saturable (Kd approximately 200 pM) and was blocked in a dose-dependent manner by the addition of intact EMAP II and unlabeled EMAP II-derived peptides (residues 6-20 and 12-20), whereas interleukin 1, tumor necrosis factor, formyl-methionyl-leucinyl-phenylalanine, or irrelevant peptides were without effect. Cross-linking of 125I-EMAP II-derived peptide (residues 12-20) by disuccinimidyl suberate to human MPs demonstrated a band, approximately 73 kDa, on reduced sodium dodecyl sulfate-polyacrylamide gel electrophoresis. 125I-EMAP II-derived peptide also demonstrated specific binding to human PMNs and murine RAW cells. These data indicate that the N-terminal region of EMAP II defines a biologically active locus of the molecule which interacts with target cells via a potentially novel cellular receptor.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
N
pubmed:pagination
9774-82
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:7545917-Amino Acid Sequence, pubmed-meshheading:7545917-Animals, pubmed-meshheading:7545917-Calcium, pubmed-meshheading:7545917-Cell Line, Transformed, pubmed-meshheading:7545917-Cell Membrane, pubmed-meshheading:7545917-Chemotaxis, Leukocyte, pubmed-meshheading:7545917-Cytokines, pubmed-meshheading:7545917-Humans, pubmed-meshheading:7545917-Inflammation, pubmed-meshheading:7545917-Kinetics, pubmed-meshheading:7545917-Leukocytes, Mononuclear, pubmed-meshheading:7545917-Macrophages, pubmed-meshheading:7545917-Mice, pubmed-meshheading:7545917-Molecular Sequence Data, pubmed-meshheading:7545917-Neoplasm Proteins, pubmed-meshheading:7545917-Neutrophils, pubmed-meshheading:7545917-Peptide Fragments, pubmed-meshheading:7545917-Peroxidase, pubmed-meshheading:7545917-Phagocytes, pubmed-meshheading:7545917-Protein Binding, pubmed-meshheading:7545917-RNA-Binding Proteins, pubmed-meshheading:7545917-Structure-Activity Relationship, pubmed-meshheading:7545917-Thromboplastin
pubmed:year
1994
pubmed:articleTitle
A peptide derived from the amino terminus of endothelial-monocyte-activating polypeptide II modulates mononuclear and polymorphonuclear leukocyte functions, defines an apparently novel cellular interaction site, and induces an acute inflammatory response.
pubmed:affiliation
Department of Physiology, Columbia University College of Physicians and Surgeons, New York, New York 10032.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't